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Simple high‐resolution NMR spectroscopy as a tool in molecular biology
Author(s) -
Mureddu Luca,
Vuister Geerten W.
Publication year - 2019
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14771
Subject(s) - biomolecule , nuclear magnetic resonance spectroscopy , computer science , simple (philosophy) , protein–protein interaction , structural biology , chemical shift , nuclear magnetic resonance spectroscopy of nucleic acids , transverse relaxation optimized spectroscopy , chemistry , computational biology , biological system , fluorine 19 nmr , biochemistry , biology , stereochemistry , philosophy , epistemology
NMR is one of the major techniques for investigating the structure, dynamics and interactions between biomolecules. However, non‐experts often experience NMR experimentation and data analysis as intimidating. We discuss a simple yet powerful NMR technique, the so‐called chemical shift perturbation ( CSP ) analysis, as a tool to elucidate macromolecular interactions in small‐ and medium‐sized complexes, including protein‐protein, protein‐drug, and protein‐ DNA / RNA interactions. We discuss current software packages for NMR data analysis and present a new interactive graphical tool implemented in CcpNmr AnalysisAssign version‐3, which can drastically reduce the time required for the CSP analysis. Lastly, we illustrate the usefulness of a protein three‐dimensional structure for interpretation of the CSP data.
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